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LOCUS NP_001027034 4178 aa linear INV 26-DEC-2023 ACCESSION NP_001027034 VERSION NP_001027034.2 DBLINK BioProject: PRJNA164 BioSample: SAMN02803731 DBSOURCE REFSEQ: accession NM_001031863.5 KEYWORDS RefSeq. SOURCE Drosophila melanogaster (fruit fly) ORGANISM Drosophila melanogaster Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora. REFERENCE 1 (residues 1 to 4178) AUTHORS Matthews,B.B., Dos Santos,G., Crosby,M.A., Emmert,D.B., St Pierre,S.E., Gramates,L.S., Zhou,P., Schroeder,A.J., Falls,K., Strelets,V., Russo,S.M. and Gelbart,W.M. CONSRTM FlyBase Consortium TITLE Gene Model Annotations for Drosophila melanogaster: Impact of High-Throughput Data JOURNAL G3 (Bethesda) 5 (8), 1721-1736 (2015) PUBMED 26109357 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 4178) AUTHORS Crosby,M.A., Gramates,L.S., Dos Santos,G., Matthews,B.B., St Pierre,S.E., Zhou,P., Schroeder,A.J., Falls,K., Emmert,D.B., Russo,S.M. and Gelbart,W.M. CONSRTM FlyBase Consortium TITLE Gene Model Annotations for Drosophila melanogaster: The Rule-Benders JOURNAL G3 (Bethesda) 5 (8), 1737-1749 (2015) PUBMED 26109356 REMARK Publication Status: Online-Only REFERENCE 3 (residues 1 to 4178) AUTHORS Hoskins,R.A., Carlson,J.W., Wan,K.H., Park,S., Mendez,I., Galle,S.E., Booth,B.W., Pfeiffer,B.D., George,R.A., Svirskas,R., Krzywinski,M., Schein,J., Accardo,M.C., Damia,E., Messina,G., Mendez-Lago,M., de Pablos,B., Demakova,O.V., Andreyeva,E.N., Boldyreva,L.V., Marra,M., Carvalho,A.B., Dimitri,P., Villasante,A., Zhimulev,I.F., Rubin,G.M., Karpen,G.H. and Celniker,S.E. TITLE The Release 6 reference sequence of the Drosophila melanogaster genome JOURNAL Genome Res 25 (3), 445-458 (2015) PUBMED 25589440 REFERENCE 4 (residues 1 to 4178) AUTHORS Hoskins,R.A., Carlson,J.W., Kennedy,C., Acevedo,D., Evans-Holm,M., Frise,E., Wan,K.H., Park,S., Mendez-Lago,M., Rossi,F., Villasante,A., Dimitri,P., Karpen,G.H. and Celniker,S.E. TITLE Sequence finishing and mapping of Drosophila melanogaster heterochromatin JOURNAL Science 316 (5831), 1625-1628 (2007) PUBMED 17569867 REFERENCE 5 (residues 1 to 4178) AUTHORS Smith,C.D., Shu,S., Mungall,C.J. and Karpen,G.H. TITLE The Release 5.1 annotation of Drosophila melanogaster heterochromatin JOURNAL Science 316 (5831), 1586-1591 (2007) PUBMED 17569856 REMARK Erratum:[Science. 2007 Sep 7;317(5843):1325] REFERENCE 6 (residues 1 to 4178) AUTHORS Quesneville,H., Bergman,C.M., Andrieu,O., Autard,D., Nouaud,D., Ashburner,M. and Anxolabehere,D. TITLE Combined evidence annotation of transposable elements in genome sequences JOURNAL PLoS Comput Biol 1 (2), 166-175 (2005) PUBMED 16110336 REFERENCE 7 (residues 1 to 4178) AUTHORS Hoskins,R.A., Smith,C.D., Carlson,J.W., Carvalho,A.B., Halpern,A., Kaminker,J.S., Kennedy,C., Mungall,C.J., Sullivan,B.A., Sutton,G.G., Yasuhara,J.C., Wakimoto,B.T., Myers,E.W., Celniker,S.E., Rubin,G.M. and Karpen,G.H. TITLE Heterochromatic sequences in a Drosophila whole-genome shotgun assembly JOURNAL Genome Biol 3 (12), RESEARCH0085 (2002) PUBMED 12537574 REFERENCE 8 (residues 1 to 4178) AUTHORS Kaminker,J.S., Bergman,C.M., Kronmiller,B., Carlson,J., Svirskas,R., Patel,S., Frise,E., Wheeler,D.A., Lewis,S.E., Rubin,G.M., Ashburner,M. and Celniker,S.E. TITLE The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective JOURNAL Genome Biol 3 (12), RESEARCH0084 (2002) PUBMED 12537573 REFERENCE 9 (residues 1 to 4178) AUTHORS Misra,S., Crosby,M.A., Mungall,C.J., Matthews,B.B., Campbell,K.S., Hradecky,P., Huang,Y., Kaminker,J.S., Millburn,G.H., Prochnik,S.E., Smith,C.D., Tupy,J.L., Whitfied,E.J., Bayraktaroglu,L., Berman,B.P., Bettencourt,B.R., Celniker,S.E., de Grey,A.D., Drysdale,R.A., Harris,N.L., Richter,J., Russo,S., Schroeder,A.J., Shu,S.Q., Stapleton,M., Yamada,C., Ashburner,M., Gelbart,W.M., Rubin,G.M. and Lewis,S.E. TITLE Annotation of the Drosophila melanogaster euchromatic genome: a systematic review JOURNAL Genome Biol 3 (12), RESEARCH0083 (2002) PUBMED 12537572 REFERENCE 10 (residues 1 to 4178) AUTHORS Celniker,S.E., Wheeler,D.A., Kronmiller,B., Carlson,J.W., Halpern,A., Patel,S., Adams,M., Champe,M., Dugan,S.P., Frise,E., Hodgson,A., George,R.A., Hoskins,R.A., Laverty,T., Muzny,D.M., Nelson,C.R., Pacleb,J.M., Park,S., Pfeiffer,B.D., Richards,S., Sodergren,E.J., Svirskas,R., Tabor,P.E., Wan,K., Stapleton,M., Sutton,G.G., Venter,C., Weinstock,G., Scherer,S.E., Myers,E.W., Gibbs,R.A. and Rubin,G.M. TITLE Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster euchromatic genome sequence JOURNAL Genome Biol 3 (12), RESEARCH0079 (2002) PUBMED 12537568 REFERENCE 11 (residues 1 to 4178) AUTHORS Adams,M.D., Celniker,S.E., Holt,R.A., Evans,C.A., Gocayne,J.D., Amanatides,P.G., Scherer,S.E., Li,P.W., Hoskins,R.A., Galle,R.F., George,R.A., Lewis,S.E., Richards,S., Ashburner,M., Henderson,S.N., Sutton,G.G., Wortman,J.R., Yandell,M.D., Zhang,Q., Chen,L.X., Brandon,R.C., Rogers,Y.H., Blazej,R.G., Champe,M., Pfeiffer,B.D., Wan,K.H., Doyle,C., Baxter,E.G., Helt,G., Nelson,C.R., Gabor,G.L., Abril,J.F., Agbayani,A., An,H.J., Andrews-Pfannkoch,C., Baldwin,D., Ballew,R.M., Basu,A., Baxendale,J., Bayraktaroglu,L., Beasley,E.M., Beeson,K.Y., Benos,P.V., Berman,B.P., Bhandari,D., Bolshakov,S., Borkova,D., Botchan,M.R., Bouck,J., Brokstein,P., Brottier,P., Burtis,K.C., Busam,D.A., Butler,H., Cadieu,E., Center,A., Chandra,I., Cherry,J.M., Cawley,S., Dahlke,C., Davenport,L.B., Davies,P., de Pablos,B., Delcher,A., Deng,Z., Mays,A.D., Dew,I., Dietz,S.M., Dodson,K., Doup,L.E., Downes,M., Dugan-Rocha,S., Dunkov,B.C., Dunn,P., Durbin,K.J., Evangelista,C.C., Ferraz,C., Ferriera,S., Fleischmann,W., Fosler,C., Gabrielian,A.E., Garg,N.S., Gelbart,W.M., Glasser,K., Glodek,A., Gong,F., Gorrell,J.H., Gu,Z., Guan,P., Harris,M., Harris,N.L., Harvey,D., Heiman,T.J., Hernandez,J.R., Houck,J., Hostin,D., Houston,K.A., Howland,T.J., Wei,M.H., Ibegwam,C., Jalali,M., Kalush,F., Karpen,G.H., Ke,Z., Kennison,J.A., Ketchum,K.A., Kimmel,B.E., Kodira,C.D., Kraft,C., Kravitz,S., Kulp,D., Lai,Z., Lasko,P., Lei,Y., Levitsky,A.A., Li,J., Li,Z., Liang,Y., Lin,X., Liu,X., Mattei,B., McIntosh,T.C., McLeod,M.P., McPherson,D., Merkulov,G., Milshina,N.V., Mobarry,C., Morris,J., Moshrefi,A., Mount,S.M., Moy,M., Murphy,B., Murphy,L., Muzny,D.M., Nelson,D.L., Nelson,D.R., Nelson,K.A., Nixon,K., Nusskern,D.R., Pacleb,J.M., Palazzolo,M., Pittman,G.S., Pan,S., Pollard,J., Puri,V., Reese,M.G., Reinert,K., Remington,K., Saunders,R.D., Scheeler,F., Shen,H., Shue,B.C., Siden-Kiamos,I., Simpson,M., Skupski,M.P., Smith,T., Spier,E., Spradling,A.C., Stapleton,M., Strong,R., Sun,E., Svirskas,R., Tector,C., Turner,R., Venter,E., Wang,A.H., Wang,X., Wang,Z.Y., Wassarman,D.A., Weinstock,G.M., Weissenbach,J., Williams,S.M., WoodageT, Worley,K.C., Wu,D., Yang,S., Yao,Q.A., Ye,J., Yeh,R.F., Zaveri,J.S., Zhan,M., Zhang,G., Zhao,Q., Zheng,L., Zheng,X.H., Zhong,F.N., Zhong,W., Zhou,X., Zhu,S., Zhu,X., Smith,H.O., Gibbs,R.A., Myers,E.W., Rubin,G.M. and Venter,J.C. TITLE The genome sequence of Drosophila melanogaster JOURNAL Science 287 (5461), 2185-2195 (2000) PUBMED 10731132 REFERENCE 12 (residues 1 to 4178) AUTHORS Celniker,S., Carlson,J., Wan,K., Pfeiffer,B., Frise,E., George,R., Hoskins,R., Stapleton,M., Pacleb,J., Park,S., Svirskas,R., Smith,E., Yu,C. and Rubin,G. CONSRTM Berkeley Drosophila Genome Project TITLE Drosophila melanogaster release 4 sequence JOURNAL Unpublished REFERENCE 13 (residues 1 to 4178) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (20-DEC-2023) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 14 (residues 1 to 4178) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (13-DEC-2023) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 15 (residues 1 to 4178) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (19-OCT-2022) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 16 (residues 1 to 4178) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (20-APR-2020) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 17 (residues 1 to 4178) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (22-APR-2019) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 18 (residues 1 to 4178) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (24-MAY-2018) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 19 (residues 1 to 4178) CONSRTM FlyBase TITLE Direct Submission JOURNAL Submitted (07-DEC-2016) FlyBase, Harvard University, Biological Laboratories, 16 Divinity Ave, Cambridge, MA 02138, USA REFERENCE 20 (residues 1 to 4178) AUTHORS Celniker,S., Carlson,J., Kennedy,C., Wan,K., Frise,E., Hoskins,R., Park,S., Svirskas,R. and Karpen,G. TITLE Direct Submission JOURNAL Submitted (10-AUG-2006) Berkeley Drosophila Genome Project, Lawrence Berkeley National Laboratory, One #Cyclotron RoadOne Cyclotron Road, MS 64-121, Berkeley, CA 94720, USA REMARK Direct Submission REFERENCE 21 (residues 1 to 4178) AUTHORS Celniker,S., Carlson,J., Wan,K., Frise,E., Hoskins,R., Park,S., Svirskas,R. and Rubin,G. TITLE Direct Submission JOURNAL Submitted (10-AUG-2006) Berkeley Drosophila Genome Project, Lawrence Berkeley National Laboratory, One Cyclotron Road, MS 64-121, Berkeley, CA 94720, USA REMARK Direct Submission REFERENCE 22 (residues 1 to 4178) AUTHORS Smith,C.D., Shu,S., Mungall,C.J. and Karpen,G.H. CONSRTM Drosophila Heterochromatin Genome Project TITLE Direct Submission JOURNAL Submitted (01-AUG-2006) Drosophila Heterochromatin Genome Project, Ernest Orlando Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Mailstop 64-121, Berkeley, CA 94720, USA REFERENCE 23 (residues 1 to 4178) AUTHORS Adams,M.D., Celniker,S.E., Gibbs,R.A., Rubin,G.M. and Venter,C.J. TITLE Direct Submission JOURNAL Submitted (21-MAR-2000) Celera Genomics, 45 West Gude Drive, Rockville, MD 20850, USA COMMENT REVIEWED REFSEQ: This record has been curated by FlyBase. The reference sequence is identical to AAN09079. On Apr 22, 2020 this sequence version replaced NP_001027034.1. ##Genome-Annotation-Data-START## Annotation Provider :: FlyBase Annotation Status :: Full annotation Annotation Version :: Release 6.54 URL :: http://flybase.org ##Genome-Annotation-Data-END## Method: conceptual translation. FEATURES Location/Qualifiers source 1..4178 /organism="Drosophila melanogaster" /db_xref="taxon:7227" /chromosome="X" /genotype="y[1]; Gr22b[1] Gr22d[1] cn[1] CG33964[R4.2] bw[1] sp[1]; LysC[1] MstProx[1] GstD5[1] Rh6[1]" Protein 1..4178 /product="terribly reduced optic lobes, isoform BB" /name="CG33950 gene product from transcript CG33950-RBB" /note="CG33950-PBB; trol-PBB; lethal (1) G0271; Trol/perlecan; mRNA-like ncRNA in embryogenesis 7; lethal (1) G0211; lethal (1) G0181; lethal (1) G0412; terribly reduced optic lobes; dPerlecan; lethal (1) G0023; lethal (1) G0374; lethal (1) G0019; lethal (1) G0021" /calculated_mol_wt=461768 Region 28..60 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(33,41,52..53) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(45,48,52,58..59) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 55..59 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 67..102 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(72,81,92..93) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(85,88,92,98..99) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 95..99 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 113..148 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(118,126,137..138) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(130,133,137,144..145) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 141..145 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 150..185 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(155,163,174..175) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(167,170,174,181..182) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 178..182 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 194..228 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(199,207,218..219) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(211,214,218,224..225) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 221..225 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 282..317 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(287,296,307..308) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(300,303,307,313..314) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 310..314 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 391..425 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(397,405,416..417) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(409,412,416,422..423) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 419..423 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 430..465 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(435,444,455..456) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(448,451,455,461..462) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 458..462 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 480..514 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(485,493,504..505) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(497,500,504,510..511) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 507..511 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 534..568 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(539,547,558..559) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(551,554,558,564..565) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 561..565 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 575..608 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(580,587,598..599) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(591,594,598,604..605) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 601..605 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 611..645 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(616,624,635..636) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(628,631,635,641..642) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 638..642 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 650..683 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(655,662,673..674) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(666,669,673,679..680) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 676..680 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 711..743 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(716,724,735..736) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(728,731,735,741..742) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 738..742 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 760..793 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(765,772,783..784) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(776,779,783,789..790) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 786..790 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 799..829 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(800,808,819..820) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(812,815,819,825..826) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 822..826 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 834..869 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(839,848,859..860) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(852,855,859,865..866) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 862..866 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 872..906 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(877,885,896..897) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(889,892,896,902..903) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 899..903 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 912..946 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(917,925,936..937) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(929,932,936,942..943) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 939..943 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 980..1015 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(985,993,1004..1005) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(997,1000,1004,1011..1012) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1008..1012 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1041..1102 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 1052..1056 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409412" Region 1066..1069 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409412" Region 1085..1089 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409412" Region 1166..1200 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(1171,1179,1190..1191) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1183,1186,1190,1196..1197) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1193..1197 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1206..1240 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(1211,1219,1230..1231) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1223,1226,1230,1236..1237) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1233..1237 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1249..1283 /region_name="LDLa" /note="Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about...; cd00112" /db_xref="CDD:238060" Site order(1254,1262,1273..1274) /site_type="active" /note="putative binding surface [active]" /db_xref="CDD:238060" Site order(1266,1269,1273,1279..1280) /site_type="other" /note="calcium-binding site [ion binding]" /db_xref="CDD:238060" Site 1276..1280 /site_type="other" /note="D-X-S-D-E motif" /db_xref="CDD:238060" Region 1301..1376 /region_name="Ig_Perlecan_like" /note="Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; cd05743" /db_xref="CDD:143220" Region 1304..1310 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:143220" Region 1317..1322 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:143220" Region 1340..1344 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:143220" Region 1353..1359 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:143220" Region 1368..1374 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:143220" Region 1475..1605 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 1662..1713 /region_name="EGF_Lam" /note="Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in...; cd00055" /db_xref="CDD:238012" Site order(1662,1664,1676,1686,1688,1697) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region 1840..1976 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region <1977..2003 /region_name="EGF_Lam" /note="Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in...; cd00055" /db_xref="CDD:238012" Region 2011..2060 /region_name="EGF_Lam" /note="Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in...; cd00055" /db_xref="CDD:238012" Site order(2012,2014,2021,2028,2031,2040) /site_type="active" /note="EGF-like motif [active]" /db_xref="CDD:238012" Region <2096..2126 /region_name="Laminin_EGF" /note="Laminin EGF domain; pfam00053" /db_xref="CDD:395007" Region 2192..2326 /region_name="Laminin_B" /note="Laminin B (Domain IV); pfam00052" /db_xref="CDD:459652" Region 2416..2484 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 2427..2431 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409412" Region 2443..2447 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409412" Region 2462..2466 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409412" Region 2476..2481 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409412" Region 2508..2578 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2607..2675 /region_name="Ig_3" /note="Immunoglobulin domain; pfam13927" /db_xref="CDD:464046" Region 2704..2788 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2721..2725 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409353" Region 2734..2738 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409353" Region 2753..2757 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409353" Region 2767..2772 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409353" Region 2780..2783 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409353" Region 2806..2879 /region_name="I-set" /note="Immunoglobulin I-set domain; pfam07679" /db_xref="CDD:400151" Region 2811..2815 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409544" Region 2824..2828 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409544" Region 2845..2849 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409544" Region 2859..2864 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409544" Region 2872..2875 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409544" Region 2882..2970 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 2902..2906 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409473" Region 2915..2919 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409473" Region 2936..2940 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409473" Region 2950..2955 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409473" Region 2963..2966 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409473" Region 3015..3072 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3018..3022 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409357" Region 3030..3033 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409357" Region 3050..3053 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409357" Region 3098..3174 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3107..3111 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409550" Region 3120..3124 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409550" Region 3154..3159 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409550" Region 3192..>3253 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3197..3201 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409412" Region 3208..3220 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409412" Region 3236..3240 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409412" Region 3302..3364 /region_name="Ig" /note="Immunoglobulin domain; cl11960" /db_xref="CDD:472250" Region 3314..3318 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409412" Region 3326..3331 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409412" Region 3347..3351 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409412" Region 3395..3461 /region_name="IG_like" /note="Immunoglobulin like; smart00410" /db_xref="CDD:214653" Region 3403..3407 /region_name="Ig strand B" /note="Ig strand B [structural motif]" /db_xref="CDD:409390" Region 3416..3420 /region_name="Ig strand C" /note="Ig strand C [structural motif]" /db_xref="CDD:409390" Region 3435..3439 /region_name="Ig strand E" /note="Ig strand E [structural motif]" /db_xref="CDD:409390" Region 3449..3454 /region_name="Ig strand F" /note="Ig strand F [structural motif]" /db_xref="CDD:409390" Region 3463..3466 /region_name="Ig strand G" /note="Ig strand G [structural motif]" /db_xref="CDD:409390" Region 3483..3628 /region_name="LamG" /note="Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of...; cd00110" /db_xref="CDD:238058" Region 3651..3683 /region_name="EGF" /note="EGF-like domain; pfam00008" /db_xref="CDD:394967" Region 3731..3884 /region_name="LamG" /note="Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of...; cd00110" /db_xref="CDD:238058" Region 3984..4137 /region_name="LamG" /note="Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of...; cd00110" /db_xref="CDD:238058" CDS 1..4178 /gene="trol" /locus_tag="Dmel_CG33950" /gene_synonym="anon-WO0153538.72; BcDNA:GM02481; CG12497; CG33675; CG33950; CG7981; CT23996; Dmel\CG33950; EG:BACR25B3.1; EG:BACR25B3.10; EG:BACR25B3.11; EG:BACR25B3.2; GC7891; l(1)3Ac; l(1)9-96; l(1)G0019; l(1)G0021; l(1)G0023; l(1)G0181; l(1)G0211; l(1)G0271; l(1)G0374; l(1)G0412; l(1)trol; l(1)VA51; l(1)zw1; l(1)zwl; MRE7; pcan; Pcan; Pcn; Perl; Perlecan; Trol; TROL; Trol-A; Trol-B; troll; Troll; zw-1; ZW-1; zw1" /coded_by="NM_001031863.5:343..12879" /db_xref="FLYBASE:FBpp0423412" /db_xref="GeneID:45320" /db_xref="FLYBASE:FBgn0284408" ORIGIN 1 msfvlschfd vdcwqclhsr ksraknkcqa nefrcnngdc idarkrcnnv sdcsegeden 61 eecpaacsgm eyqcrdgtrc isvsqqcdgh sdcsdgddee hcdgivpklr ytcpkgkftc 121 rdlscisivh rcdgradcpn drsdeegcpc lydkwqcddg tciakellcn gnidcpedis 181 deryceggyd seecrfdefh cgtgecipmr qvcdniydcn dysdevncve geeedrvgip 241 ighqpwrpas khddwlhemd tseyqvyqps nvyekansqn pcasnqfrct tsnvciplhl 301 rcdgfyhcnd msdeksceqy qrhtttrrpl tlatptsrit tqgpgllerr ntttateasr 361 wpwatkttti atttsnpitt vgvansppqt cleniefach nrdcisiesv cdgipdcgrn 421 ededdalckc sgdkykcqrg ggcipksqvc dgkpqchdrs desachlhgr lnktrlgvkc 481 lesqyqcgdg scisgykrcn gihdcadasd eynciydyed tydtdpnnnp lnecdilefe 541 cdysqclple kkcdgyadce dmsdelecqs ytdhclesef ecdsyclprd qlcngipncq 601 dgsdernctf credaylcnt gecvadnqrc ngiadcadgs derhcariyc ppnklacngt 661 cvsrrikcdg irdcldgyde mycpetnnhy ptqnvnvirp klgpnpipks crphewqcan 721 lecidsslqc neikdcsdgs deelsvcfgt attrlkpsdc speqfycdes cynrsvrcng 781 hvdcsdgsde vgcslpcpqh qcpsgrcyte sercdrhrhc edgsdeanct ailckdnefl 841 cfdrqfcina tqqcdgyydc rdfsdeqnci gcyanqfrcn ngdcvsgsap cngysecsdh 901 sdelncggtq eclpnqfrcn sgqcvsssvr cngrtdcqds sdeqncghrh tevsqglett 961 gvfttsttst tamtplriic pptsfkceng pcislglkcn grvdcpydgs deadcgqisn 1021 didpadsndr rpnqlnlkty pdsqiikesr evifrcrdeg parakvkwsr pggrplppgf 1081 tdrngrleip nirvedagty vceavgyasy ipgqqvtvnl nverswgenk yeeirsnrir 1141 ygtvphidle ffgldndvgs rpesacteyq atcmngecid kssicdgnpd csdasdeqsc 1201 slglkcqpnq fmcsnskcvd rtwrcdgend cgdnsdetsc dpepsgapcr ynefqcrsgh 1261 cipksfqcdn vpdctdgtde vgcmaplpir pppqsvslle yevleltcva tgtptptivw 1321 rlnwghvpdk cesksyggtg tlrcpdmrpq dsgaysceii ntrgthfvnp dtivtvrpvr 1381 tdvceagffn mlarkaeecv qcfcfgvaka cdsanlftya ihppilshrv vsvelsplrq 1441 ivineaapgq dlltllhgvq fratnvhfsg retpylalpa dymgnqlksy ggnlryevny 1501 rgsgrpvngp dviitgnrft ltyrvrtqpg qnnrvsipfv pggwqkpdgr kasreeimmi 1561 lanvdnilir lgyldstare vdlinialds agtadkglgs aslvekcqcp pgyvgdsces 1621 casgyvrqpg gpwlghcvpf ipdscpsgty gdprrgvpck ecpcpltgsn nfasgcqqsp 1681 dgdvvcrcne gytgrrceqc aagyqgnpla aggicrripd tscnvdgtys vhsngtcqck 1741 dsvigeqcdt cksksfhlns ftytgciecf csgvgldcds stwyrdqvts tfgrsrvdhg 1801 fvlvtnymqp tpdtvpvsma aepnalsfig sadqsgntly wslpaaflgn klssyggklt 1861 ytlsysplpn gimsrnsapd vviksgedlr lihyrksqvv psvantysve ikesawqrgd 1921 evvanrehvl malsditaiy ikatyttstk easlrqvtld vatptnlgtp raveveqcrc 1981 pegylglsce qcapgyardp eggiylglcr pcecnghsky cnsdtgdcee csdntegpsc 2041 ercaagyvgd atrgtiydcq pdegypipsp papgnqtlec taycqiegiy dcrgneclck 2101 rnvigdqcdq crpgtyglsa qnqdgckecy csglasqcrs aalyrqlipv dfilnaplit 2161 desgavqdte nlipdisrnm ytythtsylp kywslrgsvl gnqlfsyggr lsyslivesy 2221 gnyerghdiv lignglkliw srpdgnenqe eynvrlhede qwtrqdresa rpasrsdfmt 2281 vlsdlqhili ratprvptqs tsignviles avttrtpgat hasdielcqc psgyvgtsce 2341 scaplhyrda sgscslcpcd vsntescdlv sggyvecrck arwkgdrcre idtndptdig 2401 tedpvltqii vsiqkpeiti vpvggsmtls csgrmrwsns pvivnwyken srlpenvevq 2461 ggnlylydlq vsdsgvyicq avnnetasvf kdtvsititk kdqlspaeiv nlpshvtfee 2521 yvnneiicev lgnpaprvtw arvdghadaq strtydnrli fdsprksdeg ryrcqaendq 2581 nrdekyvivy vqsnppqppp qqdrlyitpe einglagesf qlncqftsva slrydwshng 2641 rslsssparn veirgntlev rdasesdsgv ytcvaydvrt rrnftesarv nidrreeqpf 2701 gnkpiiesle qniliiqged ysitceasgs pypsikwakv hdfmpenvhi sgnvltiyga 2761 rfenrgvysc vaendhgsdl sstsidiepr erpsvkivsa plqtfsvgap aslyctvegi 2821 pdptvewvrv dgqplsprhk iqspgymvid diqledsgdy ecraknivge atgvatitvq 2881 eptlvqiipd nrdlrltegd elsltcvgsg vpnpevewvn emalkrdlys ppsntailki 2941 yrvtkadagi ytchgkneag sdeahvrvev qerrgdiggv dddsdrdpin ynppqqqnpg 3001 ihqpgsnqll atdigdnvtl tcdmfqplnt rwervdgapl prnaytiknr leivrveqqn 3061 lgqyrcngig rdgnvktyfv kelvlmplpr irfypniplt veagqnldvh cqvenvrped 3121 vhwstdnnrp lpssvrivgs vlrfvsitqa aageyrcsaf nqygnrsqia rvavkkpadf 3181 hqvpqsqlqr hregeniqlq ctvtdqygvr aqdnvefnwf rddrrplpnn artdsqilvl 3241 tnlrpedagr yicnsydvdr gqqlpevsid lqvltatppp nspiylppql paksrdyslk 3301 lddqssnlra gestdvecys sddtytdvvw ersdgaplsn nvrqvgnrlv isnvspsdag 3361 nyvckcktde gdlyttsykl evedqphelk sskivyakvg anadlqcgad esrqptyrws 3421 rqygqlqagr slmneklsld svqandagty ictaqyadge tadfpnilvv tgaipqfrqe 3481 prsymsfptl pnssfkfnfe ltfrpengdg lllfngqtrg sgdyialslk dryaefrfdf 3541 ggkpmlvrae eplalnewht vrvsrfkrdg yiqvdeqhpv afptlqqipq ldliedlyig 3601 gvpnwellpa davsqqvgfv gcisrltlqg rtvelireak ykegitdcrp caqgpcqnkg 3661 vclesqteqa ytcicqpgwt grdcaiegtq ctpgvcgagr centendmec lcplnrsgdr 3721 cqyneilneh slnfkgnsfa aygtpkvtkv nitlsvrpas ledsvilyta estlpsgdyl 3781 alvlrgghae llintaarld pvvvrsaepl plnrwtriei rrrlgegilr vgdgperkak 3841 apgsdrilsl kthlyvggyd rstvkvnrdv nitkgfdgci srlynfqkpv nlladikdaa 3901 niqscgetnm iggdedsdne ppvppptpdv henelqpyam apcasdpcen ggscseqedv 3961 avcscpfgfs gkhcqehlql gfnasfrgdg yvelnrshfq paleqsytsm givfttnkpn 4021 gllfwwgqea geeytgqdfi aaavvdgyve ysmrldgeea virnsdirvd ngerhiviak 4081 rdentailev drmlhsgetr ptskksmklp gnvfvggapd levftgfryk hnlngcivvv 4141 egetvgqinl ssaavngvna nvcpanddpl ggteppvv